Regulation of p53 activity by its interaction with homeodomain-interacting protein kinase-2

@article{Hofmann2002RegulationOP,
  title={Regulation of p53 activity by its interaction with homeodomain-interacting protein kinase-2},
  author={Thomas G. Hofmann and Andreas M{\"o}ller and Hüseyin Sirma and H. Zentgraf and Yoichi Taya and Wulf Dröge and Hans Will and Michael Lienhard Schmitz},
  journal={Nature Cell Biology},
  year={2002},
  volume={4},
  pages={1-10}
}
Transcriptional activity of p53, a central regulatory switch in a network controlling cell proliferation and apoptosis, is modulated by protein stability and post-translational modifications including phosphorylation and acetylation. Here we demonstrate that the human serine/threonine kinase homeodomain-interacting protein kinase-2 (HIPK2) colocalizes and interacts with p53 and CREB-binding protein (CBP) within promyelocytic leukaemia (PML) nuclear bodies. HIPK2 is activated by ultraviolet (UV… 
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The results suggest that the critical apoptosis regulator KAISO is a p53 target gene that is differently regulated by phosphorylated p53 or acetylated p53, depending on DDR stage.
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